1F70: Calmodulin N-terminal domain

Refined solution structure of calmodulin N-terminal domain. Determined by solution NMR. Released 22 Sept 2000.

Method
Solution NMR
Organism
Xenopus laevis
Chains
1
Atoms
588
Mol. weight
8.45 kDa
Released
22 Sept 2000

Explore 1F70 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1F70 contains 6 α-helices and 2 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 6 helices, 2 β-strands

ElementResiduesLengthSheet
α-helix3-53
α-helix6-1813
β-strand26-2831
α-helix29-313
α-helix32-398
α-helix45-5511
β-strand62-6431
α-helix65-7511

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
CalmodulinAprotein76Xenopus laevisP0DP33 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1F70_1 CALMODULIN (chains A)
ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGN
GTIDFPEFLTMMARKM

Primary citation

Study of conformational rearrangement and refinement of structural homology models by the use of heteronuclear dipolar couplings. Chou, J.J., Li, S., Bax, A. J Biomol NMR (2000) 18:217-227. DOI 10.1023/A:1026563923774 · PubMed

Other PDB entries of the same protein (UniProt P0DP33 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

About this viewer

MolViewer shows 1F70 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.